4g2d | pdb_00004g2d

Crystal structure of the hyperthermophilic Sulfolobus islandicus PLL SisLac

spinqualitylabelsall models 4g2d, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g2d is a 1 chain structure with sequence from Sulfolobus islandicus M.16.4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: CO, FE2, KCX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4KKZ9_SULIK Publication Abstract from PubMed BACKGROUND: A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa. METHODOLOGY/PRINCIPAL FINDINGS: Here, we describe the substrate specificity of SisLac, providing extensive kinetic studies performed with various phosphotriesters, esters, N-acyl-homoserine lactones (AHLs) and other lactones as substrates. Moreover, we solved the X-ray structure of SisLac and structural comparisons with the closely related SsoPox structure highlighted differences in the surface salt bridge network and the dimerization interface. SisLac and SsoPox being close homologues (91% sequence identity), we undertook a mutational study to decipher these structural differences and their putative consequences on the stability and the catalytic properties of these proteins. CONCLUSIONS/SIGNIFICANCE: We show that SisLac is a very proficient lactonase against aroma lactones and AHLs as substrates. Hence, data herein emphasize the potential role of SisLac as quorum quenching agent in Sulfolobus. Moreover, despite the very high sequence homology with SsoPox, we highlight key epistatic substitutions that influence the enzyme stability and activity. Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.,Hiblot J, Gotthard G, Chabriere E, Elias M PLoS One. 2012;7(10):e47028. doi: 10.1371/journal.pone.0047028. Epub 2012 Oct 10. PMID:23071703 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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